en>Citation bot 1: [Pu408]Add: doi. You can use this bot yourself. Report bugs here.

2011-10-06T22:17:00Z

[Pu408]Add: doi. You can use this bot yourself. Report bugs here.

New page

{{enzyme
| Name = L-fucose isomerase
| EC_number = 5.3.1.25
| CAS_number = 60063-83-4
| IUBMB_EC_number = 5/3/1/25
| GO_code = 0008736
| image =
| width =
| caption =
}}
{{Infobox protein family
| Symbol = Fucose_iso_N1
| Name = L-fucose isomerase, first N-terminal domain
| image = PDB 1fui EBI.jpg
| width =
| caption = l-fucose isomerase from escherichia coli
| Pfam = PF07881
| Pfam_clan =
| InterPro = IPR012888
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1fui
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = Fucose_iso_N2
| Name = L-fucose isomerase, second N-terminal domain
| image = PDB 1fui EBI.jpg
| width =
| caption = l-fucose isomerase from escherichia coli
| Pfam = PF07882
| Pfam_clan =
| InterPro = IPR012889
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1fui
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
{{Infobox protein family
| Symbol = Fucose_iso_C
| Name = L-fucose isomerase, C-terminal domain
| image = PDB 1fui EBI.jpg
| width =
| caption = l-fucose isomerase from escherichia coli
| Pfam = PF02952
| Pfam_clan = CL0393
| InterPro = IPR015888
| SMART =
| PROSITE =
| MEROPS =
| SCOP = 1fui
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
In [[enzymology]], a '''L-fucose isomerase''' ({{EC number|5.3.1.25}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]

:L-fucose <math>\rightleftharpoons</math> L-fuculose

Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[L-fucose]], and one [[product (chemistry)|product]], [[L-fuculose]].

This enzyme belongs to the family of [[isomerase]]s, specifically those intramolecular [[oxidoreductase]]s interconverting [[aldose]]s and [[ketose]]s. The systematic name of this enzyme class is '''L-fucose aldose-ketose-isomerase'''. This enzyme participates in [[Fructose metabolism|fructose]] and [[Mannose metabolism|mannose metabolism]].

The [[enzyme]] is a hexamer, forming the largest [[structurally]] known [[ketol]] [[isomerase]], and has no [[sequence (biology)|sequence]] or [[secondary structure|structural]] similarity with other ketol isomerases. The [[secondary structure|structure]] was determined by [[X-ray crystallography]] at 2.5 [[Angstrom]] resolution.<ref name="pmid9367760">{{cite journal | author = Seemann JE, Schulz GE | title = Structure and mechanism of L-fucose isomerase from Escherichia coli | journal = J. Mol. Biol. | volume = 273 | issue = 1 | pages = 256–68 |date=October 1997 | pmid = 9367760 | doi = 10.1006/jmbi.1997.1280 | url = }}</ref> Each subunit of the hexameric enzyme is wedge-shaped and composed of three [[protein domain|domains]]. Both [[protein domains|domains]] 1 and 2 contain central parallel beta- [[beta sheet|sheets]] with surrounding [[alpha helix|alpha helices]]. The active centre is shared between pairs of [[protein subunit|subunits]] related along the molecular three-fold axis, with domains 2 and 3 from one subunit providing most of the substrate-contacting [[Residue (chemistry)|residue]]s.<ref name="pmid9367760" />

==References==
{{reflist}}
==Further reading==
{{reflist|1}}
* {{cite journal | author = Lu Z, Lin EC | year = 1989 | title = The nucleotide sequence of Escherichia coli genes for L-fucose dissimilation | journal = Nucleic. Acids. Res. | volume = 17 | pages = 4883–4 | pmid = 2664711 | doi = 10.1093/nar/17.12.4883 | issue = 12 | pmc = 318048 }}

{{isomerase-stub}}
{{InterPro content|IPR015888}}

{{InterPro content|IPR012889}}

{{InterPro content|IPR012888}}

[[Category:Protein domains]]
[[Category:EC 5.3.1]]
[[Category:Enzymes of unknown structure]]

Isocitrate epimerase - Revision history

en>Citation bot 1: [Pu408]Add: doi. You can use this bot yourself. Report bugs here.